Vol.3, No.1, 35-38 (2012) Journ al of Biophysical Chemistry
An interactive 3D viewer of molecules compatible
with the suite of ANTHEPROT programs
Gilbert Deléage
Unité Bases Moléculaires et Structurales des Systèmes Infectieux, UMR 5086 CNRS, Université Claude Bernard Lyon 1, Lyon,
France; gilbert.deleage@ibcp.fr
Received 11 October 2011; revised 3 December 2011; accepted 17 December 2011
In this p aper, I will describe a completely ne w 3D
module which can be called from within the well
known ANTHEPROT program devoted to protein
sequences analysis. This module allows fully
interactive handling of high-quality 3D struc-
tures with various modes of representation (CA
sticks, wireframe, ball and sticks, spacefill mod-
els as well as surface, ribbons, Ramachandran
plots). Alternatively, ANTHEPROT 3D can be
used as an external program fully independant
from the global package. It is available from the
download page of the web site
(http://antheprot-pbil.ibcp.fr/). More than 2800
downloads last year were recorded since the
program was delivered.
Keywords: Protein; Sequence Analysis; Structural
Bioinformatics; Software; 3D Structures
Many programs [1-7] or Web servers [8-10] exist for
the visualisation of th e 3D structure of protein s. Howeve r,
few of them have some possibilities for sequence analy-
sis [7,11]. In the 90’s, we have proposed one of the very
first package for the analysis of protein sequence [12].
For over 20 years, this software has been continuoulsy
updated for various plateforms including Apple II, Mac-
Intosh, DOS [13] and AIX (IBM unix) operating system
in the 1990’s [14-16]. In the latest published version,
which is designed for the Windows OS, several im-
provements were made such as the addition of a client-
server mode [17] for distant submissions that takes ad-
vantage of remote servers hosting databases regularly
updated [18]. However, at that time, no effective 3D
module was associated with the program.
In this article, I describe a completely new version of
the program ANTHEPROT 3D that allows interactive
manipulation of 3D structures of proteins. The program
is mainly devoted to th e comprehensive understand ing of
biological molecules by viewing their 3D structures. It
includes all the standard functions found in other 3D
viewers. The main originality is that it can be launched
directly from the main window of the widely used AN-
THEPROT program designed for the analysis of protein
sequence. A gallery showing the possibilities of this
module is available at http://antheprot-pbil.ibcp.fr/3D.
ANTHEPROT 3D program is a completely new pro-
gram for Windows interface, which uses the OpenGL 3D
library. So, the program performs best on computers that
have OpenGL graphic cards but also works on any card
(in a quite performant emulation mode). The program is
available, as a complete ready-to-run archive file. An
help file (ANTHE.HLP file) is also present in the pack-
age. The program can also be considered as an interface
for several well known external programs, such as the
MSMS molecular surface for surface calculation [19],
the ribbon molscript program [20], the DSSP program for
secondary structure calculation [21], the DELPHI algo-
rithm for electrostatic potential calculations [22] and
“REDUCE” program for hydrogen additi on/rem oval [23] .
ANTHEPROT 3D consists of 4 different panels (Fig-
ure 1). The first one (Figure 1(a)) is the OpenGL win-
dow for the graphical display. The manipulation of the
molecule can be achieved by a trackball emulation mode
that can be activated or deactivated in real time. This
feature allows a very precise manipulation of the mole-
cule or, alternatively, the discovery of the molecule with
a flying mode. Once a PDB file is loaded, the secondary
structures are calculated on the fly using the DSSP algo-
rithm [21], the CA trace is shown in this window as
sticks colored by chain (default). Two other related win-
dows are displayed: one (Figure 1(b)) is used to provide
a list of amino acids from which the selection of the
esidues can be made in a multiple selection mode. The r
Copyright © 2012 SciRes. OPEN ACCESS
G. Deléage / Journal of Biophysical Chemistry 3 (2 012) 35-38
Figure 1. Program main interface. (a) The main window for viewing molecule (pdb code: 3SGB). The electrostatic potential is dis-
played (positive potential in blue and negative one in red) onto the MSMS surface; (b) The window amino acid list for selection; (c)
The information window; (d) The Ramachandran window. An arrow indicates the current position in the sequence.
third window (Figure 1(c)) is used to provide the user
with useful information (distances, angles, global content
in secondary structure, phi/spi angles, sequences, number
of chains, number of atoms). The program is fully cus-
tomisable for color codes (amino acid groups, chains,
atoms, hydrophobic/hydrophilic residues, B factor, elec-
trostatic potential) that can be combined with conven-
tional modes of representation (CA backbone, wireframe,
sticks, ball and sticks, spacefill, ribbons and surface).
The graphics quality can be adjusted so as to provide a
good compromise between quality and speed of execu-
tion depending upon the molecule size and the type of
graphic card.
The program allows the display of large molecules.
Indeed, Figure 2 shows the surface of a viral capsid
(2BUK), rendered in a solid Gouraud mode, colored by
subunits. It should be noted that even in this mode, the
interactivity is preserved. Alternatively, the grid surface
can be calculated and the transparency of the surface can
be adjusted with a slider. This surface can be still interac-
tively handled on a machine equiped with graphic cards
supporting OpenGL. ANTHEPROT can display onto the
MSMS surface the electrostatic potential calculated by
using the external program DELPHI. The manipulation
of the molecule in the graphics window is still fully in-
teractive using a virtual trackball for rotation, zooming
and moving. Moreover, the program has selection capa-
bilities through the picking of atoms for identification of
parent residues, distance between atoms, angles and tor-
sion angles.
ANTHEPROT 3D also offers a selection mode of
amino acids within a sphere, the radius of which can be
adjus ted on the fly by the user. The f ar and near clipping
plans can also be interactively adjusted. An interactive
Ramachandran plot is also available (Figure 1(d)) which
allows to display the phi, psi angles, the list of angles and
an panel showing the corresponding sequence and sec-
ondary structure. This panel can be updated after picking
a point in a region of the Ramachandran surface or
moved backward or forward by using the arrows of the
Copyright © 2012 SciRes. OPEN ACCESS
G. Deléage / Journal of Biophysical Chemistry 3 (2 012) 35-38 37
Figure 2. MSMS surface rendering in ANTHEPROT 3D view-
ing program. Pdb code: 2BUK (from the biological unit file
from PDB).
keyboard. In all cases, both sequence and secondary
structure around the current position is updated. This
original tool is very useful to connect the sequence of a
protein, its secondary structure and the 3D display. For
example, when a PDB file is loaded from within the pro-
gram for protein sequence analysis, the sequence of the
protein is automatically extracted and provided in the
sequence module. This allows to enter into this sequence
program from a 3D structure. So, the ANTHEPROT 3D
can be considered as an optional module to the classical
ANTHEPROT program.
Another useful tool is the complete support of interac-
tive multiple stereo views. Among the supported modes,
the classic mode with two views side by side (crossed
eyes), the anaglyph red/green stereo mode, the quad-
buffer mode which needs polarized screen and passive
glasses, and the interlaced row mode suitable for flat
screens such as stereo Zalman.
Some examples of several kinds of representations of-
fered by ANTHEPROT 3D are given in Figure 3. More-
over to take advantage of the important functions pro-
vided by other programs, ANTHEPROT 3D is able to
launch some external programs, transparen tly to the user.
For the display of ribbons (Figure 3(b)), ANTHEPROT
3D is able to generate input files for Molauto/MOL-
SCRIPT and it is able to exploit the output files gener-
ated by these two programs. Helices can be shown in
“cartoons” mode (alternatively helices can be represented
as cigars that give their N and C orientations). The addi-
tion/suppression of hydrogens is performed by using a
Figure 3. Examples of views obtained with ANTHEPROT
3D. (a) Alpha carbon view of 5HMG in colored subunits;
(b) Moscript view of 1MAX; (c) Spacefill colored atom
view of hydrogenated 1MBJ; (d) Transparent grid surface
of 1CRN.
call to the “REDUCE” program (Figure 3(c)). Surface
calculation can be performed in a fully transparent man-
ner with the help of the widely used MSMS algorithm
(Figure 3(d)).
The program can also generate video recording from
the assembly of regularly dumped images. In order to
illustrate the capabilities of the program a gallery web
site is visible at http://antheprot-pbil.ibcp.fr/3D.
Although many 3D protein viewers exist, to my know-
ledge, ANTHEPROT is the unique program that was
primarily devoted to protein sequence analysis (with a lot
of tools such as matrix dot-plot, multiple alignements,
secondary structure prediction) that also allows a power-
ful rendering of the 3D structure of protein. That is why
this completely new 3D module was written in order to
allow 3D structure handling from within the ANTHE-
PROT sequence software. As a consequence, it should
not be considered as a additional modelling tool but
rather as a vizualisation tool coupled to a sequence ana-
lysis program. Efforts have been made in order to facili-
tate the discovery of proteins organisation through the
CA default mode. In this context, the user-friendly inter-
face has been enhanced by the implementation of a
Copyright © 2012 SciRes. OPEN ACCESS
G. Deléage / Journal of Biophysical Chemistry 3 (2 012) 35-38
Copyright © 2012 SciRes.
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experience in the program or in-depth knowledge of the
3D structure of proteins. The ANTHEPROT 3D program
is freely available and, during the last 12 months 2888
downloads of the software have been registered. Possible
developments include a specialisation of the module to-
wards protein interaction interface visualisation and ana-
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Thanks are due to Dr. Ramon Yáñez López (University of Barcelona)
for providing me some pieces of code for centering molecule and to
CNRS and Lyon University for supporting this work.
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